Hematopoietic Disorders, Renal Impairment and Growth in Mucopolysaccharidosis-Plus Syndrome.

Mucopolysaccharidoses (MPS) are rare lysosomal storage disorders (LSD) characterized by the excessive accumulation of glycosaminoglycans (GAG). Conventional MPS, caused by inborn deficiencies of lysosomal enzymes involved in GAG degradation, display various multisystemic symptoms-including progressive neurological complications, ophthalmological disorders, hearing loss, gastrointestinal and hepatobiliary issues, cardiorespiratory problems, bone and joint abnormalities, dwarfism, and coarse facial features. Mucopolysaccharidosis-Plus Syndrome (MPSPS), an autosomal recessive disease caused by a mutation in the endo-lysosomal tethering protein VPS33A, shows additional renal and hematopoietic abnormalities ("Plus symptoms") uncommon in conventional MPS.

[Effect of RGD-containing peptides on platelet aggregation].

The influence of new synthetic peptides ARGDS-NH2 and RGD-dFK (synthesized by the fermentative method) and VPNLRGDLQVLA (a fragment of the foot-and-mouth virus's surface peptide) on the ADP-induced human platelet aggregation in vitro was studied. All peptides were found to inhibit the human platelet aggregation, but the synthetic peptides (ARGDS-NH2 and RGD-dFK) showed the most pronounced effect. Significant decrease in the platelet aggregation was observed at their concentrations within 0.

[Characterization of S1' subsite specificity of Thermoactinomyces vulgaris carboxypeptidase T by site-directed mutagenesis].

The site-directed mutagenesis in the S1'-pocket of Thermoactinomyces vulgaris carboxypeptidase T was performed and two variants containing double D253S, T255D and single T255D mutations were obtained. Precursors of the wild-type carboxypeptidase T and its mutant derivatives were expressed in Escherichia coli as inclusion bodies, refolded, activated by subtilisin, purified by gel efiltration on Superdex G-75. The catalytic activity with tripeptide substrates DNPAAR and ZAAL was analysed.

[Sequential attachment of arginine residues to peptides catalyzed by subtilisin. II. Effect of the nature of acylating and nucleophilic components and small amounts of water in organic solvents].

The reaction of Dnp(or Z)-Ala2-Xaa-OCH3 (Xaa = Ile of Val) with arginine amide or p-nitroanilide was studied in organic solvents, which was catalyzed by subtilisin sorbed on macroporous glass, It resulted in the formation of peptides containing one to four arginine residues: Dnp(or Z)-Ala2-Xaa-(Arg) 1-4-NH2. The number of arginine residues attached to the peptide depended on the water content in organic solvents, nature of the amino acid residue Xaa in the P1 position of the acylating component, and the type of the N-protective group. The reaction can be used for synthesizing arginine-containing substrates of convertases and cathepsins B, L, and O.

[Sequential attachment of arginine residues to peptides, catalyzed by subtilisin. 1. Effect of organic solvent composition].

Subtilisin 72 sorbed on a macroporous glass catalyzed the condensation of Dnp(or Z)-Ala2-Leu-OCH3 with arginine amide in a mixture of DMSO and acetonitrile at a water content less than 0.07% (v/v). This reaction resulted in the sequential formation of peptides containing from one to four C-terminal arginine residues.